3mha

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{{STRUCTURE_3mha| PDB=3mha | SCENE= }}
 
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===Crystal structure of LprG from Mycobacterium tuberculosis bound to PIM===
 
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{{ABSTRACT_PUBMED_20694006}}
 
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==Function==
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==Crystal structure of LprG from Mycobacterium tuberculosis bound to PIM==
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[[http://www.uniprot.org/uniprot/LPRG_MYCTU LPRG_MYCTU]] TLR2 agonist that can inhibit primary human macrophage MHC-II Ag processing. Required for Rv1410c (P55) activity.<ref>PMID:15294983</ref> <ref>PMID:18156250</ref>
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<StructureSection load='3mha' size='340' side='right'caption='[[3mha]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3mha]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MHA FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=Z69:(1S,2R,3R,4S,5R,6S)-2-(alpha-L-allopyranosyloxy)-3,4,5-trihydroxy-6-({6-O-[(1R)-1-hydroxyhexadecyl]-beta-L-gulopyranosyl}oxy)cyclohexyl+(2R)-2-{[(1S)-1-hydroxyhexadecyl]oxy}-3-{[(1S,10S)-1-hydroxy-10-methyloctadecyl]oxy}propyl+hydrogen+(R)-phosphate'>Z69</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mha OCA], [https://pdbe.org/3mha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mha RCSB], [https://www.ebi.ac.uk/pdbsum/3mha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mha ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LPRG_MYCTU LPRG_MYCTU] TLR2 agonist that can inhibit primary human macrophage MHC-II Ag processing. Required for Rv1410c (P55) activity.<ref>PMID:15294983</ref> <ref>PMID:18156250</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mh/3mha_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3mha ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Knockout of lprG results in decreased virulence of Mycobacterium tuberculosis (MTB) in mice. MTB lipoprotein LprG has TLR2 agonist activity, which is thought to be dependent on its N-terminal triacylation. Unexpectedly, here we find that nonacylated LprG retains TLR2 activity. Moreover, we show LprG association with triacylated glycolipid TLR2 agonists lipoarabinomannan, lipomannan and phosphatidylinositol mannosides (which share core structures). Binding of triacylated species was specific to LprG (not LprA) and increased LprG TLR2 agonist activity; conversely, association of glycolipids with LprG enhanced their recognition by TLR2. The crystal structure of LprG in complex with phosphatidylinositol mannoside revealed a hydrophobic pocket that accommodates the three alkyl chains of the ligand. In conclusion, we demonstrate a glycolipid binding function of LprG that enhances recognition of triacylated MTB glycolipids by TLR2 and may affect glycolipid assembly or transport for bacterial cell wall biogenesis.
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==About this Structure==
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Mycobacterium tuberculosis lipoprotein LprG (Rv1411c) binds triacylated glycolipid agonists of Toll-like receptor 2.,Drage MG, Tsai HC, Pecora ND, Cheng TY, Arida AR, Shukla S, Rojas RE, Seshadri C, Moody DB, Boom WH, Sacchettini JC, Harding CV Nat Struct Mol Biol. 2010 Aug 8. PMID:20694006<ref>PMID:20694006</ref>
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[[3mha]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MHA OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:020694006</ref><references group="xtra"/><references/>
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</div>
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[[Category: Mycobacterium tuberculosis]]
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<div class="pdbe-citations 3mha" style="background-color:#fffaf0;"></div>
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[[Category: Sacchettini, J C.]]
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== References ==
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[[Category: TBSGC, TB Structural Genomics Consortium.]]
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<references/>
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[[Category: Tsai, H C.]]
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__TOC__
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[[Category: Glycolipid binding protein]]
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</StructureSection>
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[[Category: Lipid binding protein]]
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[[Category: Large Structures]]
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[[Category: Lipoprotein]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Lprg]]
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[[Category: Sacchettini JC]]
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[[Category: Structural genomic]]
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[[Category: Tsai H-C]]
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[[Category: Tb structural genomics consortium]]
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[[Category: Tbsgc]]
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Current revision

Crystal structure of LprG from Mycobacterium tuberculosis bound to PIM

PDB ID 3mha

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